Molecular adaptation to calsequestrin 2 (CASQ2) point mutations leading to catecholaminergic polymorphic ventricular tachycardia (CPVT): comparative analysis of R33Q and D307H mutants

Giorgia Valle, Michael Arad, Pompeo Volpe*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Homozygous calsequestrin 2 (CASQ2) point mutations leads to catecholaminergic polymorphic ventricular tachycardia: a common pathogenetic feature appears to be the drastic reduction of mutant CASQ2 in spite of normal transcription. Comparative biochemical analysis of R33Q and D307H knock in mutant mice identifies different pathogenetic mechanisms for CASQ2 degradation and different molecular adaptive mechanisms. In particular, each CASQ2 point mutation evokes specific adaptive cellular and molecular processes in each of the four adaptive pathways investigated. Thus, similar clinical phenotypes and identical cellular mechanism for cardiac arrhythmia might imply different molecular adaptive mechanisms.

Original languageEnglish
Pages (from-to)251-258
Number of pages8
JournalJournal of Muscle Research and Cell Motility
Volume41
Issue number2-3
DOIs
StatePublished - Sep 2020

Funding

FundersFunder number
Telethon ONLUS FoundationGGP11141
Università degli Studi di Padova
Israel Science Foundation763/10

    Keywords

    • CASQ2 mutations
    • Cathecolaminergic polymorphic ventricular tachycardia
    • Degradative pathways
    • Small heat shock proteins

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